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P15692

- VEGFA_HUMAN

UniProt

P15692 - VEGFA_HUMAN

Protein

Vascular endothelial growth factor A

Gene

VEGFA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 195 (01 Oct 2014)
      Sequence version 2 (16 Nov 2001)
      Previous versions | rss
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    Functioni

    Growth factor active in angiogenesis, vasculogenesis and endothelial cell growth. Induces endothelial cell proliferation, promotes cell migration, inhibits apoptosis and induces permeabilization of blood vessels. Binds to the FLT1/VEGFR1 and KDR/VEGFR2 receptors, heparan sulfate and heparin. NRP1/Neuropilin-1 binds isoforms VEGF-165 and VEGF-145. Isoform VEGF165B binds to KDR but does not activate downstream signaling pathways, does not activate angiogenesis and inhibits tumor growth.2 Publications

    GO - Molecular functioni

    1. chemoattractant activity Source: UniProtKB
    2. cytokine activity Source: BHF-UCL
    3. extracellular matrix binding Source: BHF-UCL
    4. fibronectin binding Source: BHF-UCL
    5. growth factor activity Source: BHF-UCL
    6. heparin binding Source: UniProtKB
    7. identical protein binding Source: IntAct
    8. neuropilin binding Source: BHF-UCL
    9. platelet-derived growth factor receptor binding Source: BHF-UCL
    10. protein binding Source: IntAct
    11. protein heterodimerization activity Source: MGI
    12. protein homodimerization activity Source: BHF-UCL
    13. receptor agonist activity Source: BHF-UCL
    14. vascular endothelial growth factor receptor 1 binding Source: BHF-UCL
    15. vascular endothelial growth factor receptor 2 binding Source: BHF-UCL
    16. vascular endothelial growth factor receptor binding Source: UniProtKB

    GO - Biological processi

    1. activation of protein kinase activity Source: BHF-UCL
    2. angiogenesis Source: UniProtKB
    3. artery morphogenesis Source: BHF-UCL
    4. basophil chemotaxis Source: UniProtKB
    5. blood coagulation Source: Reactome
    6. branching morphogenesis of an epithelial tube Source: BHF-UCL
    7. camera-type eye morphogenesis Source: BHF-UCL
    8. cardiac muscle fiber development Source: BHF-UCL
    9. cardiac vascular smooth muscle cell development Source: BHF-UCL
    10. cell maturation Source: BHF-UCL
    11. cell migration involved in sprouting angiogenesis Source: BHF-UCL
    12. cellular response to hypoxia Source: MGI
    13. cellular response to vascular endothelial growth factor stimulus Source: BHF-UCL
    14. commissural neuron axon guidance Source: BHF-UCL
    15. coronary artery morphogenesis Source: BHF-UCL
    16. coronary vein morphogenesis Source: BHF-UCL
    17. dopaminergic neuron differentiation Source: BHF-UCL
    18. endothelial cell chemotaxis Source: BHF-UCL
    19. epithelial cell differentiation Source: BHF-UCL
    20. eye photoreceptor cell development Source: BHF-UCL
    21. growth Source: BHF-UCL
    22. heart morphogenesis Source: BHF-UCL
    23. induction of positive chemotaxis Source: UniProtKB
    24. in utero embryonic development Source: BHF-UCL
    25. kidney development Source: BHF-UCL
    26. lactation Source: BHF-UCL
    27. lung development Source: BHF-UCL
    28. lymph vessel morphogenesis Source: BHF-UCL
    29. macrophage differentiation Source: DFLAT
    30. mammary gland alveolus development Source: BHF-UCL
    31. mesoderm development Source: BHF-UCL
    32. monocyte differentiation Source: DFLAT
    33. negative regulation of apoptotic process Source: UniProtKB
    34. negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
    35. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    36. nervous system development Source: UniProtKB
    37. outflow tract morphogenesis Source: BHF-UCL
    38. ovarian follicle development Source: BHF-UCL
    39. patterning of blood vessels Source: BHF-UCL
    40. platelet activation Source: Reactome
    41. platelet degranulation Source: Reactome
    42. positive chemotaxis Source: BHF-UCL
    43. positive regulation of angiogenesis Source: UniProtKB
    44. positive regulation of axon extension involved in axon guidance Source: BHF-UCL
    45. positive regulation of blood vessel endothelial cell migration Source: BHF-UCL
    46. positive regulation of branching involved in ureteric bud morphogenesis Source: BHF-UCL
    47. positive regulation of cell adhesion Source: UniProtKB
    48. positive regulation of cell division Source: UniProtKB-KW
    49. positive regulation of cell migration Source: BHF-UCL
    50. positive regulation of cell migration involved in sprouting angiogenesis Source: BHF-UCL
    51. positive regulation of cell proliferation Source: BHF-UCL
    52. positive regulation of cell proliferation by VEGF-activated platelet derived growth factor receptor signaling pathway Source: BHF-UCL
    53. positive regulation of cellular component movement Source: BHF-UCL
    54. positive regulation of CREB transcription factor activity Source: BHF-UCL
    55. positive regulation of endothelial cell chemotaxis by VEGF-activated vascular endothelial growth factor receptor signaling pathway Source: BHF-UCL
    56. positive regulation of endothelial cell migration Source: UniProtKB
    57. positive regulation of endothelial cell proliferation Source: UniProtKB
    58. positive regulation of epithelial cell proliferation Source: BHF-UCL
    59. positive regulation of ERK1 and ERK2 cascade Source: BHF-UCL
    60. positive regulation of focal adhesion assembly Source: UniProtKB
    61. positive regulation of gene expression Source: UniProtKB
    62. positive regulation of histone deacetylase activity Source: BHF-UCL
    63. positive regulation of intracellular signal transduction Source: BHF-UCL
    64. positive regulation of leukocyte migration Source: BHF-UCL
    65. positive regulation of MAP kinase activity Source: BHF-UCL
    66. positive regulation of mast cell chemotaxis Source: UniProtKB
    67. positive regulation of mesenchymal cell proliferation Source: BHF-UCL
    68. positive regulation of neuroblast proliferation Source: BHF-UCL
    69. positive regulation of p38MAPK cascade Source: UniProtKB
    70. positive regulation of peptidyl-serine phosphorylation Source: BHF-UCL
    71. positive regulation of peptidyl-tyrosine autophosphorylation Source: BHF-UCL
    72. positive regulation of peptidyl-tyrosine phosphorylation Source: BHF-UCL
    73. positive regulation of positive chemotaxis Source: BHF-UCL
    74. positive regulation of protein autophosphorylation Source: BHF-UCL
    75. positive regulation of protein complex assembly Source: UniProtKB
    76. positive regulation of protein kinase C signaling Source: BHF-UCL
    77. positive regulation of protein localization to early endosome Source: BHF-UCL
    78. positive regulation of protein phosphorylation Source: UniProtKB
    79. positive regulation of receptor internalization Source: BHF-UCL
    80. positive regulation of retinal ganglion cell axon guidance Source: BHF-UCL
    81. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    82. positive regulation of transcription from RNA polymerase II promoter in response to hypoxia Source: BHF-UCL
    83. positive regulation of vascular endothelial growth factor receptor signaling pathway Source: BHF-UCL
    84. positive regulation of vascular permeability Source: UniProtKB
    85. post-embryonic camera-type eye development Source: BHF-UCL
    86. primitive erythrocyte differentiation Source: BHF-UCL
    87. regulation of cell shape Source: BHF-UCL
    88. regulation of retinal ganglion cell axon guidance Source: BHF-UCL
    89. regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    90. regulation of transcription from RNA polymerase II promoter in response to hypoxia Source: Reactome
    91. response to hypoxia Source: UniProtKB
    92. surfactant homeostasis Source: BHF-UCL
    93. tube formation Source: UniProtKB
    94. vascular endothelial growth factor receptor signaling pathway Source: BHF-UCL
    95. vascular endothelial growth factor signaling pathway Source: BHF-UCL
    96. vasculogenesis Source: UniProtKB
    97. VEGF-activated neuropilin signaling pathway Source: BHF-UCL

    Keywords - Molecular functioni

    Developmental protein, Growth factor, Mitogen

    Keywords - Biological processi

    Angiogenesis, Differentiation

    Keywords - Ligandi

    Heparin-binding

    Enzyme and pathway databases

    ReactomeiREACT_121092. Regulation of gene expression by Hypoxia-inducible Factor.
    REACT_12380. VEGF ligand-receptor interactions.
    REACT_12583. VEGF binds to VEGFR leading to receptor dimerization.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Vascular endothelial growth factor A
    Short name:
    VEGF-A
    Alternative name(s):
    Vascular permeability factor
    Short name:
    VPF
    Gene namesi
    Name:VEGFA
    Synonyms:VEGF
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:12680. VEGFA.

    Subcellular locationi

    Secreted 3 Publications
    Note: VEGF121 is acidic and freely secreted. VEGF165 is more basic, has heparin-binding properties and, although a signicant proportion remains cell-associated, most is freely secreted. VEGF189 is very basic, it is cell-associated after secretion and is bound avidly by heparin and the extracellular matrix, although it may be released as a soluble form by heparin, heparinase or plasmin.

    GO - Cellular componenti

    1. cell surface Source: BHF-UCL
    2. cytoplasm Source: UniProtKB
    3. extracellular region Source: Reactome
    4. extracellular space Source: UniProtKB
    5. membrane Source: InterPro
    6. platelet alpha granule lumen Source: Reactome
    7. proteinaceous extracellular matrix Source: UniProtKB
    8. secretory granule Source: UniProtKB

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Microvascular complications of diabetes 1 (MVCD1) [MIM:603933]: Pathological conditions that develop in numerous tissues and organs as a consequence of diabetes mellitus. They include diabetic retinopathy, diabetic nephropathy leading to end-stage renal disease, and diabetic neuropathy. Diabetic retinopathy remains the major cause of new-onset blindness among diabetic adults. It is characterized by vascular permeability and increased tissue ischemia and angiogenesis.
    Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.

    Organism-specific databases

    MIMi603933. phenotype.
    PharmGKBiPA37302.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 26262 PublicationsAdd
    BLAST
    Chaini27 – 232206Vascular endothelial growth factor APRO_0000023386Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi52 ↔ 94
    Disulfide bondi77 – 77Interchain
    Disulfide bondi83 ↔ 128
    Disulfide bondi86 – 86Interchain
    Disulfide bondi87 ↔ 130
    Glycosylationi101 – 1011N-linked (GlcNAc...)

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiP15692.
    PRIDEiP15692.

    PTM databases

    PhosphoSiteiP15692.

    Expressioni

    Tissue specificityi

    Isoform VEGF189, isoform VEGF165 and isoform VEGF121 are widely expressed. Isoform VEGF206 and isoform VEGF145 are not widely expressed. A higher level expression seen in pituitary tumors as compared to the pituitary gland.1 Publication

    Inductioni

    By hypoxia. Regulated by growth factors, cytokines, gonadotropins, nitric oxide, hypoglycemia and oncogenic mutations.1 Publication

    Gene expression databases

    ArrayExpressiP15692.
    BgeeiP15692.
    GenevestigatoriP15692.

    Organism-specific databases

    HPAiCAB005429.

    Interactioni

    Subunit structurei

    Homodimer; disulfide-linked. Also found as heterodimer with PGF By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself9EBI-1026643,EBI-1026643
    FLT1P179484EBI-1026643,EBI-1026718
    KDRP359685EBI-1026691,EBI-1005487
    NRP1O147864EBI-1026643,EBI-1187100
    NRP1O14786-24EBI-1026691,EBI-6285281

    Protein-protein interaction databases

    BioGridi113265. 27 interactions.
    DIPiDIP-5740N.
    IntActiP15692. 16 interactions.
    MINTiMINT-2834049.

    Structurei

    Secondary structure

    1
    232
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi43 – 508
    Beta strandi51 – 6010
    Helixi61 – 644
    Helixi66 – 683
    Beta strandi71 – 8414
    Beta strandi93 – 10917
    Turni111 – 1133
    Beta strandi116 – 13116
    Beta strandi189 – 1913
    Beta strandi194 – 1974
    Turni199 – 2013
    Beta strandi204 – 2085
    Helixi210 – 2145
    Turni215 – 2173
    Beta strandi219 – 2213
    Turni222 – 2243
    Beta strandi226 – 2283

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BJ1X-ray2.40V/W34-135[»]
    1CZ8X-ray2.40V/W40-133[»]
    1FLTX-ray1.70V/W38-135[»]
    1KATNMR-V/W37-135[»]
    1KMXNMR-A183-232[»]
    1MJVX-ray2.10A/B40-134[»]
    1MKGX-ray2.50A/B/C/D40-134[»]
    1MKKX-ray1.32A/B40-134[»]
    1QTYX-ray2.70R/S/V/W34-135[»]
    1TZHX-ray2.60V/W34-135[»]
    1TZIX-ray2.80V34-135[»]
    1VGHNMR-A180-232[»]
    1VPFX-ray2.50A/B/C/D34-135[»]
    1VPPX-ray1.90V/W34-135[»]
    2FJGX-ray2.80V/W34-135[»]
    2FJHX-ray3.10V/W34-135[»]
    2QR0X-ray3.50C/D/I/J/O/P/U/V39-135[»]
    2VGHNMR-A182-232[»]
    2VPFX-ray1.93A/B/C/D/E/F/G/H34-135[»]
    3BDYX-ray2.60V34-135[»]
    3P9WX-ray2.41A/C/E/G35-138[»]
    3QTKX-ray1.85A/B/C/D/E/F34-135[»]
    3S1BX-ray2.90V38-133[»]
    3S1KX-ray2.55V/W34-135[»]
    3V2AX-ray3.20A27-140[»]
    4DEQX-ray2.65A/B183-232[»]
    4GLNX-ray1.60E/F34-135[»]
    4GLSX-ray1.60E/F34-135[»]
    4KZNX-ray1.71A39-135[»]
    ProteinModelPortaliP15692.
    SMRiP15692. Positions 39-133, 183-232.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP15692.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the PDGF/VEGF growth factor family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG73329.
    HOVERGENiHBG000105.
    InParanoidiP15692.
    KOiK05448.
    PhylomeDBiP15692.

    Family and domain databases

    Gene3Di2.10.160.10. 1 hit.
    2.10.90.10. 1 hit.
    InterProiIPR029034. Cystine-knot_cytokine.
    IPR023581. PD_growth_factor_CS.
    IPR000072. PDGF/VEGF_dom.
    IPR027928. VEGF_C.
    [Graphical view]
    PfamiPF00341. PDGF. 1 hit.
    PF14554. VEGF_C. 1 hit.
    [Graphical view]
    SMARTiSM00141. PDGF. 1 hit.
    [Graphical view]
    SUPFAMiSSF57501. SSF57501. 1 hit.
    SSF57593. SSF57593. 1 hit.
    PROSITEiPS00249. PDGF_1. 1 hit.
    PS50278. PDGF_2. 1 hit.
    [Graphical view]

    Sequences (17)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 17 isoformsi produced by alternative promoter usage, alternative splicing and alternative initiation. Align

    Note: Additional isoforms seem to exist.

    Isoform VEGF206 (identifier: P15692-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MNFLLSWVHW SLALLLYLHH AKWSQAAPMA EGGGQNHHEV VKFMDVYQRS    50
    YCHPIETLVD IFQEYPDEIE YIFKPSCVPL MRCGGCCNDE GLECVPTEES 100
    NITMQIMRIK PHQGQHIGEM SFLQHNKCEC RPKKDRARQE KKSVRGKGKG 150
    QKRKRKKSRY KSWSVYVGAR CCLMPWSLPG PHPCGPCSER RKHLFVQDPQ 200
    TCKCSCKNTD SRCKARQLEL NERTCRCDKP RR 232
    Length:232
    Mass (Da):27,042
    Last modified:November 16, 2001 - v2
    Checksum:iFB49F364446F4D01
    GO
    Isoform VEGF189 (identifier: P15692-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         166-182: Missing.

    Show »
    Length:215
    Mass (Da):25,173
    Checksum:i7B9759AD5871FF33
    GO
    Isoform VEGF183 (identifier: P15692-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         160-182: Missing.

    Show »
    Length:209
    Mass (Da):24,422
    Checksum:iF01CCEACD945D6CA
    GO
    Isoform VEGF165 (identifier: P15692-4) [UniParc]FASTAAdd to Basket

    Also known as: VEGF

    The sequence of this isoform differs from the canonical sequence as follows:
         141-141: K → N
         142-182: Missing.

    Show »
    Length:191
    Mass (Da):22,314
    Checksum:iCCE57097DD3779BD
    GO
    Isoform VEGF148 (identifier: P15692-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         141-141: K → N
         142-182: Missing.
         215-215: A → M
         216-232: Missing.

    Show »
    Length:174
    Mass (Da):20,218
    Checksum:iAE88400CA7757644
    GO
    Isoform VEGF145 (identifier: P15692-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         166-226: Missing.

    Show »
    Length:171
    Mass (Da):20,064
    Checksum:iD02ECA735FF6E9F8
    GO
    Isoform VEGF165B (identifier: P15692-8) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         141-141: K → N
         142-182: Missing.
         227-232: CDKPRR → SLTRKD

    Show »
    Length:191
    Mass (Da):22,259
    Checksum:iD25243E540AC79BD
    GO
    Isoform VEGF121 (identifier: P15692-9) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         142-226: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:147
    Mass (Da):17,219
    Checksum:iDDF4D6994249BED6
    GO
    Isoform VEGF111 (identifier: P15692-10) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         132-226: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:137
    Mass (Da):15,981
    Checksum:i196B2BB49381BE87
    GO
    Isoform L-VEGF165 (identifier: P15692-11) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MTDRQTDTAP...AGPGRASETM
         141-141: K → N
         142-182: Missing.

    Note: Produced by alternative promoter usage and alternative initiation. Starts at an alternative upstream CUG codon. Post-translationally processed to produce the secreted VEGF peptide and a N-terminal peptide N-VEGF. The unprocessed protein and the N-VEGF peptide may localize to the nucleus (PubMed:15896327), the endoplasmic reticulum and the Golgi (PubMed:11731620) or the extracellular matrix (PubMed:11563986).3 Publications

    Show »
    Length:371
    Mass (Da):40,738
    Checksum:i053E9CA56725C07B
    GO
    Isoform L-VEGF121 (identifier: P15692-12) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MTDRQTDTAP...AGPGRASETM
         142-226: Missing.

    Note: Produced by alternative promoter usage and alternative initiation. Starts at an alternative upstream CUG codon. Post-translationally processed to produce the secreted VEGF peptide and a N-terminal peptide N-VEGF. The unprocessed protein and the N-VEGF peptide may localize to the nucleus (PubMed:15896327), the endoplasmic reticulum and the Golgi (PubMed:11731620) or the extracellular matrix (PubMed:11563986).3 Publications

    Show »
    Length:327
    Mass (Da):35,643
    Checksum:i8D6F969601B2A9EF
    GO
    Isoform L-VEGF189 (identifier: P15692-13) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MTDRQTDTAP...AGPGRASETM
         166-182: Missing.

    Note: Produced by alternative promoter usage and alternative initiation. Starts at an alternative upstream CUG codon. Post-translationally processed to produce the secreted VEGF peptide and a N-terminal peptide N-VEGF. The unprocessed protein and the N-VEGF peptide may localize to the nucleus (PubMed:15896327), the endoplasmic reticulum and the Golgi (PubMed:11731620) or the extracellular matrix (PubMed:11563986).3 Publications

    Show »
    Length:395
    Mass (Da):43,597
    Checksum:i8ADF6524B1835A2D
    GO
    Isoform L-VEGF206 (identifier: P15692-14) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MTDRQTDTAP...AGPGRASETM

    Note: Gene prediction based on EST data. Produced by alternative promoter usage and alternative initiation. Starts at an alternative upstream CUG codon.

    Show »
    Length:412
    Mass (Da):45,467
    Checksum:iAC807D3F21528D35
    GO
    Isoform 15 (identifier: P15692-15) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MTDRQTDTAP...AGPGRASETM
         141-182: KKSVRGKGKGQKRKRKKSRYKSWSVYVGARCCLMPWSLPGPH → N
         227-232: CDKPRR → SLTRKD

    Note: Starts at an alternative upstream CUG codon.

    Show »
    Length:371
    Mass (Da):40,683
    Checksum:i1B89AFD7FABEC07B
    GO
    Isoform 16 (identifier: P15692-16) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MTDRQTDTAP...AGPGRASETM
         160-182: Missing.

    Note: Starts at an alternative upstream CUG codon.

    Show »
    Length:389
    Mass (Da):42,846
    Checksum:i950279CF7A273A0E
    GO
    Isoform 17 (identifier: P15692-17) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MTDRQTDTAP...AGPGRASETM
         141-182: KKSVRGKGKGQKRKRKKSRYKSWSVYVGARCCLMPWSLPGPH → N
         215-215: A → M
         216-232: Missing.

    Note: Starts at an alternative upstream CUG codon.

    Show »
    Length:354
    Mass (Da):38,642
    Checksum:i0152409399BAB1EB
    GO
    Isoform 18 (identifier: P15692-18) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MTDRQTDTAP...AGPGRASETM
         132-226: Missing.

    Note: Starts at an alternative upstream CUG codon.

    Show »
    Length:317
    Mass (Da):34,406
    Checksum:iFDF27C1251E3B613
    GO

    Sequence cautioni

    The sequence AAC63143.1 differs from that shown. Reason: Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.
    The sequence CAC19512.2 differs from that shown. Reason: Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.
    The sequence CAC19516.2 differs from that shown. Reason: Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.
    The sequence AAC63102.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti87 – 871C → S in AAC63143. (PubMed:9450968)Curated
    Sequence conflicti210 – 2101D → H in AAC63143. (PubMed:9450968)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MTDRQTDTAPSPSYHLLPGR RRTVDAAASRGQGPEPAPGG GVEGVGARGVALKLFVQLLG CSRFGGAVVRAGEAEPSGAA RSASSGREEPQPEEGEEEEE KEEERGPQWRLGARKPGSWT GEAAVCADSAPAARAPQALA RASGRGGRVARRGAEESGPP HSPSRRGSASRAGPGRASET M in isoform L-VEGF165, isoform L-VEGF121, isoform L-VEGF189, isoform L-VEGF206, isoform 15, isoform 16, isoform 17 and isoform 18. 1 PublicationVSP_038745
    Alternative sequencei132 – 22695Missing in isoform VEGF111 and isoform 18. 1 PublicationVSP_026781Add
    BLAST
    Alternative sequencei141 – 18242KKSVR…LPGPH → N in isoform 15 and isoform 17. CuratedVSP_054111Add
    BLAST
    Alternative sequencei141 – 1411K → N in isoform VEGF148, isoform VEGF165, isoform VEGF165B and isoform L-VEGF165. 10 PublicationsVSP_004618
    Alternative sequencei142 – 22685Missing in isoform VEGF121 and isoform L-VEGF121. 1 PublicationVSP_004620Add
    BLAST
    Alternative sequencei142 – 18241Missing in isoform VEGF148, isoform VEGF165, isoform VEGF165B and isoform L-VEGF165. 10 PublicationsVSP_004619Add
    BLAST
    Alternative sequencei160 – 18223Missing in isoform VEGF183 and isoform 16. 2 PublicationsVSP_004621Add
    BLAST
    Alternative sequencei166 – 22661Missing in isoform VEGF145. 1 PublicationVSP_004623Add
    BLAST
    Alternative sequencei166 – 18217Missing in isoform VEGF189 and isoform L-VEGF189. 2 PublicationsVSP_004622Add
    BLAST
    Alternative sequencei215 – 2151A → M in isoform VEGF148 and isoform 17. 1 PublicationVSP_004624
    Alternative sequencei216 – 23217Missing in isoform VEGF148 and isoform 17. 1 PublicationVSP_004625Add
    BLAST
    Alternative sequencei227 – 2326CDKPRR → SLTRKD in isoform VEGF165B and isoform 15. 1 PublicationVSP_014783

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M32977 mRNA. Translation: AAA35789.1.
    M27281 mRNA. Translation: AAA36807.1.
    M63978
    , M63971, M63972, M63973, M63974, M63975, M63976, M63977 Genomic DNA. Translation: AAA36804.1.
    S85192 mRNA. Translation: AAC63102.1. Different initiation.
    AH006909 Genomic DNA. Translation: AAC63101.1.
    X62568 mRNA. Translation: CAA44447.1.
    AJ010438 mRNA. Translation: CAA09179.1.
    AF022375 mRNA. Translation: AAC63143.1. Sequence problems.
    AF091352 mRNA. Translation: AAD55345.1.
    AF430806 mRNA. Translation: AAL27435.1.
    AB021221 mRNA. Translation: BAA78418.1.
    AF214570 mRNA. Translation: AAF19659.1.
    AY047581 mRNA. Translation: AAK95847.1.
    AF486837 mRNA. Translation: AAM03108.1.
    AY766116 mRNA. Translation: AAV34601.1.
    DQ229900 mRNA. Translation: ABB58912.1.
    AB451322 mRNA. Translation: BAG70136.1.
    AB451451 mRNA. Translation: BAG70265.1.
    AL136131 Genomic DNA. Translation: CAC19512.2. Sequence problems.
    AL136131 Genomic DNA. Translation: CAC19513.2.
    AL136131 Genomic DNA. Translation: CAC19515.2.
    AL136131 Genomic DNA. Translation: CAC19516.2. Sequence problems.
    CH471081 Genomic DNA. Translation: EAX04229.1.
    BC065522 mRNA. Translation: AAH65522.2.
    AF437895 Genomic DNA. Translation: AAL27630.1.
    AF062645 mRNA. Translation: AAC16730.1.
    CCDSiCCDS34457.1. [P15692-14]
    CCDS34458.1. [P15692-11]
    CCDS47432.1. [P15692-15]
    CCDS47433.1. [P15692-16]
    CCDS47434.1. [P15692-12]
    CCDS47435.1. [P15692-17]
    CCDS4907.2. [P15692-13]
    CCDS55007.1. [P15692-18]
    CCDS55008.1. [P15692-3]
    CCDS55009.1. [P15692-2]
    CCDS55010.1. [P15692-1]
    CCDS55011.1. [P15692-5]
    CCDS55012.1. [P15692-4]
    CCDS55013.1. [P15692-8]
    CCDS55014.1. [P15692-9]
    CCDS55015.1. [P15692-10]
    PIRiA41551.
    RefSeqiNP_001020537.2. NM_001025366.2. [P15692-14]
    NP_001020538.2. NM_001025367.2. [P15692-16]
    NP_001020539.2. NM_001025368.2. [P15692-11]
    NP_001020540.2. NM_001025369.2. [P15692-17]
    NP_001020541.2. NM_001025370.2. [P15692-12]
    NP_001028928.1. NM_001033756.2. [P15692-15]
    NP_001165093.1. NM_001171622.1. [P15692-18]
    NP_001165094.1. NM_001171623.1. [P15692-1]
    NP_001165095.1. NM_001171624.1. [P15692-2]
    NP_001165096.1. NM_001171625.1. [P15692-3]
    NP_001165097.1. NM_001171626.1. [P15692-4]
    NP_001165098.1. NM_001171627.1. [P15692-5]
    NP_001165099.1. NM_001171628.1. [P15692-9]
    NP_001165100.1. NM_001171629.1. [P15692-8]
    NP_001165101.1. NM_001171630.1. [P15692-10]
    NP_001191313.1. NM_001204384.1. [P15692-6]
    NP_001191314.1. NM_001204385.1.
    NP_001273973.1. NM_001287044.1.
    NP_003367.4. NM_003376.5. [P15692-13]
    UniGeneiHs.73793.

    Genome annotation databases

    EnsembliENST00000372077; ENSP00000361148; ENSG00000112715. [P15692-9]
    ENST00000457104; ENSP00000409911; ENSG00000112715. [P15692-10]
    ENST00000518689; ENSP00000430829; ENSG00000112715. [P15692-3]
    ENST00000518824; ENSP00000430002; ENSG00000112715. [P15692-8]
    ENST00000520948; ENSP00000428321; ENSG00000112715. [P15692-2]
    ENST00000523125; ENSP00000429008; ENSG00000112715. [P15692-5]
    ENST00000523873; ENSP00000430479; ENSG00000112715. [P15692-1]
    ENST00000523950; ENSP00000429643; ENSG00000112715. [P15692-4]
    GeneIDi7422.
    KEGGihsa:7422.
    UCSCiuc003owd.3. human. [P15692-5]
    uc003owe.3. human. [P15692-4]
    uc003owf.3. human. [P15692-13]
    uc003owg.3. human. [P15692-3]
    uc003owh.3. human. [P15692-1]
    uc003owi.3. human. [P15692-8]
    uc003owj.3. human. [P15692-9]
    uc010jyx.3. human. [P15692-10]

    Polymorphism databases

    DMDMi17380528.

    Keywords - Coding sequence diversityi

    Alternative initiation, Alternative promoter usage, Alternative splicing

    Cross-referencesi

    Web resourcesi

    R&D Systems' cytokine mini-reviews: VEGF
    Wikipedia

    VEGF entry

    SeattleSNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M32977 mRNA. Translation: AAA35789.1 .
    M27281 mRNA. Translation: AAA36807.1 .
    M63978
    , M63971 , M63972 , M63973 , M63974 , M63975 , M63976 , M63977 Genomic DNA. Translation: AAA36804.1 .
    S85192 mRNA. Translation: AAC63102.1 . Different initiation.
    AH006909 Genomic DNA. Translation: AAC63101.1 .
    X62568 mRNA. Translation: CAA44447.1 .
    AJ010438 mRNA. Translation: CAA09179.1 .
    AF022375 mRNA. Translation: AAC63143.1 . Sequence problems.
    AF091352 mRNA. Translation: AAD55345.1 .
    AF430806 mRNA. Translation: AAL27435.1 .
    AB021221 mRNA. Translation: BAA78418.1 .
    AF214570 mRNA. Translation: AAF19659.1 .
    AY047581 mRNA. Translation: AAK95847.1 .
    AF486837 mRNA. Translation: AAM03108.1 .
    AY766116 mRNA. Translation: AAV34601.1 .
    DQ229900 mRNA. Translation: ABB58912.1 .
    AB451322 mRNA. Translation: BAG70136.1 .
    AB451451 mRNA. Translation: BAG70265.1 .
    AL136131 Genomic DNA. Translation: CAC19512.2 . Sequence problems.
    AL136131 Genomic DNA. Translation: CAC19513.2 .
    AL136131 Genomic DNA. Translation: CAC19515.2 .
    AL136131 Genomic DNA. Translation: CAC19516.2 . Sequence problems.
    CH471081 Genomic DNA. Translation: EAX04229.1 .
    BC065522 mRNA. Translation: AAH65522.2 .
    AF437895 Genomic DNA. Translation: AAL27630.1 .
    AF062645 mRNA. Translation: AAC16730.1 .
    CCDSi CCDS34457.1. [P15692-14 ]
    CCDS34458.1. [P15692-11 ]
    CCDS47432.1. [P15692-15 ]
    CCDS47433.1. [P15692-16 ]
    CCDS47434.1. [P15692-12 ]
    CCDS47435.1. [P15692-17 ]
    CCDS4907.2. [P15692-13 ]
    CCDS55007.1. [P15692-18 ]
    CCDS55008.1. [P15692-3 ]
    CCDS55009.1. [P15692-2 ]
    CCDS55010.1. [P15692-1 ]
    CCDS55011.1. [P15692-5 ]
    CCDS55012.1. [P15692-4 ]
    CCDS55013.1. [P15692-8 ]
    CCDS55014.1. [P15692-9 ]
    CCDS55015.1. [P15692-10 ]
    PIRi A41551.
    RefSeqi NP_001020537.2. NM_001025366.2. [P15692-14 ]
    NP_001020538.2. NM_001025367.2. [P15692-16 ]
    NP_001020539.2. NM_001025368.2. [P15692-11 ]
    NP_001020540.2. NM_001025369.2. [P15692-17 ]
    NP_001020541.2. NM_001025370.2. [P15692-12 ]
    NP_001028928.1. NM_001033756.2. [P15692-15 ]
    NP_001165093.1. NM_001171622.1. [P15692-18 ]
    NP_001165094.1. NM_001171623.1. [P15692-1 ]
    NP_001165095.1. NM_001171624.1. [P15692-2 ]
    NP_001165096.1. NM_001171625.1. [P15692-3 ]
    NP_001165097.1. NM_001171626.1. [P15692-4 ]
    NP_001165098.1. NM_001171627.1. [P15692-5 ]
    NP_001165099.1. NM_001171628.1. [P15692-9 ]
    NP_001165100.1. NM_001171629.1. [P15692-8 ]
    NP_001165101.1. NM_001171630.1. [P15692-10 ]
    NP_001191313.1. NM_001204384.1. [P15692-6 ]
    NP_001191314.1. NM_001204385.1.
    NP_001273973.1. NM_001287044.1.
    NP_003367.4. NM_003376.5. [P15692-13 ]
    UniGenei Hs.73793.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BJ1 X-ray 2.40 V/W 34-135 [» ]
    1CZ8 X-ray 2.40 V/W 40-133 [» ]
    1FLT X-ray 1.70 V/W 38-135 [» ]
    1KAT NMR - V/W 37-135 [» ]
    1KMX NMR - A 183-232 [» ]
    1MJV X-ray 2.10 A/B 40-134 [» ]
    1MKG X-ray 2.50 A/B/C/D 40-134 [» ]
    1MKK X-ray 1.32 A/B 40-134 [» ]
    1QTY X-ray 2.70 R/S/V/W 34-135 [» ]
    1TZH X-ray 2.60 V/W 34-135 [» ]
    1TZI X-ray 2.80 V 34-135 [» ]
    1VGH NMR - A 180-232 [» ]
    1VPF X-ray 2.50 A/B/C/D 34-135 [» ]
    1VPP X-ray 1.90 V/W 34-135 [» ]
    2FJG X-ray 2.80 V/W 34-135 [» ]
    2FJH X-ray 3.10 V/W 34-135 [» ]
    2QR0 X-ray 3.50 C/D/I/J/O/P/U/V 39-135 [» ]
    2VGH NMR - A 182-232 [» ]
    2VPF X-ray 1.93 A/B/C/D/E/F/G/H 34-135 [» ]
    3BDY X-ray 2.60 V 34-135 [» ]
    3P9W X-ray 2.41 A/C/E/G 35-138 [» ]
    3QTK X-ray 1.85 A/B/C/D/E/F 34-135 [» ]
    3S1B X-ray 2.90 V 38-133 [» ]
    3S1K X-ray 2.55 V/W 34-135 [» ]
    3V2A X-ray 3.20 A 27-140 [» ]
    4DEQ X-ray 2.65 A/B 183-232 [» ]
    4GLN X-ray 1.60 E/F 34-135 [» ]
    4GLS X-ray 1.60 E/F 34-135 [» ]
    4KZN X-ray 1.71 A 39-135 [» ]
    ProteinModelPortali P15692.
    SMRi P15692. Positions 39-133, 183-232.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113265. 27 interactions.
    DIPi DIP-5740N.
    IntActi P15692. 16 interactions.
    MINTi MINT-2834049.

    Chemistry

    BindingDBi P15692.
    ChEMBLi CHEMBL1783.
    DrugBanki DB01076. Atorvastatin.
    DB00112. Bevacizumab.
    DB01136. Carvedilol.
    DB01381. Ginkgo biloba.
    DB01120. Gliclazide.
    DB01017. Minocycline.
    DB01270. Ranibizumab.
    DB00641. Simvastatin.
    GuidetoPHARMACOLOGYi 2644.

    PTM databases

    PhosphoSitei P15692.

    Polymorphism databases

    DMDMi 17380528.

    Proteomic databases

    PaxDbi P15692.
    PRIDEi P15692.

    Protocols and materials databases

    DNASUi 7422.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000372077 ; ENSP00000361148 ; ENSG00000112715 . [P15692-9 ]
    ENST00000457104 ; ENSP00000409911 ; ENSG00000112715 . [P15692-10 ]
    ENST00000518689 ; ENSP00000430829 ; ENSG00000112715 . [P15692-3 ]
    ENST00000518824 ; ENSP00000430002 ; ENSG00000112715 . [P15692-8 ]
    ENST00000520948 ; ENSP00000428321 ; ENSG00000112715 . [P15692-2 ]
    ENST00000523125 ; ENSP00000429008 ; ENSG00000112715 . [P15692-5 ]
    ENST00000523873 ; ENSP00000430479 ; ENSG00000112715 . [P15692-1 ]
    ENST00000523950 ; ENSP00000429643 ; ENSG00000112715 . [P15692-4 ]
    GeneIDi 7422.
    KEGGi hsa:7422.
    UCSCi uc003owd.3. human. [P15692-5 ]
    uc003owe.3. human. [P15692-4 ]
    uc003owf.3. human. [P15692-13 ]
    uc003owg.3. human. [P15692-3 ]
    uc003owh.3. human. [P15692-1 ]
    uc003owi.3. human. [P15692-8 ]
    uc003owj.3. human. [P15692-9 ]
    uc010jyx.3. human. [P15692-10 ]

    Organism-specific databases

    CTDi 7422.
    GeneCardsi GC06P043737.
    HGNCi HGNC:12680. VEGFA.
    HPAi CAB005429.
    MIMi 192240. gene.
    603933. phenotype.
    neXtProti NX_P15692.
    PharmGKBi PA37302.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG73329.
    HOVERGENi HBG000105.
    InParanoidi P15692.
    KOi K05448.
    PhylomeDBi P15692.

    Enzyme and pathway databases

    Reactomei REACT_121092. Regulation of gene expression by Hypoxia-inducible Factor.
    REACT_12380. VEGF ligand-receptor interactions.
    REACT_12583. VEGF binds to VEGFR leading to receptor dimerization.

    Miscellaneous databases

    ChiTaRSi VEGFA. human.
    EvolutionaryTracei P15692.
    GeneWikii Vascular_endothelial_growth_factor_A.
    GenomeRNAii 7422.
    NextBioi 29060.
    PROi P15692.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P15692.
    Bgeei P15692.
    Genevestigatori P15692.

    Family and domain databases

    Gene3Di 2.10.160.10. 1 hit.
    2.10.90.10. 1 hit.
    InterProi IPR029034. Cystine-knot_cytokine.
    IPR023581. PD_growth_factor_CS.
    IPR000072. PDGF/VEGF_dom.
    IPR027928. VEGF_C.
    [Graphical view ]
    Pfami PF00341. PDGF. 1 hit.
    PF14554. VEGF_C. 1 hit.
    [Graphical view ]
    SMARTi SM00141. PDGF. 1 hit.
    [Graphical view ]
    SUPFAMi SSF57501. SSF57501. 1 hit.
    SSF57593. SSF57593. 1 hit.
    PROSITEi PS00249. PDGF_1. 1 hit.
    PS50278. PDGF_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Vascular endothelial growth factor is a secreted angiogenic mitogen."
      Leung D.W., Cachianes G., Kuang W.-J., Goeddel D.V., Ferrara N.
      Science 246:1306-1309(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS VEGF189 AND VEGF165).
    2. "Vascular permeability factor, an endothelial cell mitogen related to PDGF."
      Keck P.J., Hauser S.D., Krivi G., Sanzo K., Warren T., Feder J., Connolly D.T.
      Science 246:1309-1312(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VEGF189), PARTIAL PROTEIN SEQUENCE.
    3. "The human gene for vascular endothelial growth factor. Multiple protein forms are encoded through alternative exon splicing."
      Tischer E., Mitchell R., Hartman T., Silva M., Gospodarowicz D., Fiddes J.C., Abraham J.A.
      J. Biol. Chem. 266:11947-11954(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM VEGF189).
    4. "The vascular endothelial growth factor family: identification of a fourth molecular species and characterization of alternative splicing of RNA."
      Houck K.A., Ferrara N., Winer J., Cachianes G., Li B., Leung D.W.
      Mol. Endocrinol. 5:1806-1814(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM VEGF206).
    5. "AIDS-associated Kaposi's sarcoma cells in culture express vascular endothelial growth factor."
      Weindel K., Marme D., Weich H.A.
      Biochem. Biophys. Res. Commun. 183:1167-1174(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VEGF165).
    6. "VEGF145, a secreted vascular endothelial growth factor isoform that binds to extracellular matrix."
      Poltorak Z., Cohen T., Sivan R., Kandelis Y., Spira G., Vlodavsky I., Keshet E., Neufeld G.
      J. Biol. Chem. 272:7151-7158(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VEGF145).
    7. "Identification and characterization of a new splicing variant of vascular endothelial growth factor: VEGF183."
      Lei J., Jiang A., Pei D.
      Biochim. Biophys. Acta 1443:400-406(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VEGF183).
      Tissue: Kidney.
    8. "Identification of a human VPF/VEGF 3' untranslated region mediating hypoxia-induced mRNA stability."
      Claffey K.P., Shih S.-C., Mullen A., Dziennis S., Cusick J.L., Abrams K.R., Lee S.W., Detmar M.
      Mol. Biol. Cell 9:469-481(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM L-VEGF165).
      Tissue: Mammary gland.
    9. "Heterogeneous vascular endothelial growth factor (VEGF) isoform mRNA and receptor mRNA expression in human glomeruli, and the identification of VEGF148 mRNA, a novel truncated splice variant."
      Whittle C.J., Gillespie K.M., Harrison R., Mathieson P.W., Harper S.J.
      Clin. Sci. 97:303-312(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VEGF148).
      Tissue: Renal glomerulus.
    10. "VEGF165b, an inhibitory splice variant of vascular endothelial growth factor, is down-regulated in renal cell carcinoma."
      Bates D.O., Cui T.-G., Doughty J.M., Winkler M., Sugiono M., Shields J.D., Peat D., Gillatt D., Harper S.J.
      Cancer Res. 62:4123-4131(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VEGF165B).
      Tissue: Kidney.
    11. "Human cDNA for the vascular endothelial growth factor isoform VEGF165."
      Murata H., Fukushima J., Hattori S., Okuda K., Yanagi H.
      Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VEGF165).
      Tissue: Hemangioendothelioma.
    12. "Human cDNA for vascular endothelial growth factor isoform VEGF121."
      Sato J.D., Whitney R.G.
      Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VEGF121).
    13. "Cloning of vascular endothelial growth factor (VEGF) cDNA."
      Liu J., Peng X., Yuan J., Qiang B.
      Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VEGF165).
    14. "Cloning and identification of vascular endothelial growth factor isoform VEGF165."
      Shan Z.X., Yu X.Y., Lin Q.X., Fu Y.H., Zheng M., Tan H.H., Lin S.G.
      Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VEGF165).
      Tissue: Heart.
    15. "Cloning and characterization of VEGF from LNCaP cells, a line of prostate cancer cells."
      Koul S., Johnson T., Meacham R.B., Koul H.K.
      Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VEGF165).
    16. "VEGF111, a new VEGF-A variant lacking exons 5, 6 and 7."
      Mineur P.J., Colige A.C., Lambert C.A.
      Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VEGF111).
    17. "Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
      Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.
      , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
      Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM VEGF165).
    18. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    19. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    20. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM L-VEGF121).
      Tissue: Lung.
    21. SeattleSNPs variation discovery resource
      Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 23-232.
    22. "Synthesis and assembly of functionally active human vascular endothelial growth factor homodimers in insect cells."
      Fiebich B.L., Jaeger B., Schoellmann C., Weindel K., Wilting J., Kochs G., Marme D., Hug H., Weich H.A.
      Eur. J. Biochem. 211:19-26(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 27-41.
    23. "Signal peptide prediction based on analysis of experimentally verified cleavage sites."
      Zhang Z., Henzel W.J.
      Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 27-41.
    24. "Human vascular permeability factor. Isolation from U937 cells."
      Connolly D.T., Olander J.V., Heuvelman D., Nelson R., Monsell R., Siegel N., Haymore B.L., Leimgruber R., Feder J.
      J. Biol. Chem. 264:20017-20024(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PRELIMINARY PROTEIN SEQUENCE OF 27-36; 43-50 AND 59-81.
    25. "Human Muller cells express VEGF183, a novel spliced variant of vascular endothelial growth factor."
      Jingjing L., Xue Y., Agarwal N., Roque R.S.
      Invest. Ophthalmol. Vis. Sci. 40:752-759(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 114-209 (ISOFORM VEGF183).
      Tissue: Retina.
    26. "A precursor form of vascular endothelial growth factor arises by initiation from an upstream in-frame CUG codon."
      Tee M.K., Jaffe R.B.
      Biochem. J. 359:219-226(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING (ISOFORMS L-VEGF121 AND L-VEGF165), PROCESSING, SUBCELLULAR LOCATION.
    27. "Vascular endothelial growth factor induces cyclooxygenase-dependent proliferation of endothelial cells via the VEGF-2 receptor."
      Murphy J.F., Fitzgerald D.J.
      FASEB J. 15:1667-1669(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    28. "New vascular endothelial growth factor isoform generated by internal ribosome entry site-driven CUG translation initiation."
      Huez I., Bornes S., Bresson D., Creancier L., Prats H.
      Mol. Endocrinol. 15:2197-2210(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING (ISOFORM L-VEGF189), PROCESSING, SUBCELLULAR LOCATION.
    29. "A common polymorphism in the 5'-untranslated region of the VEGF gene is associated with diabetic retinopathy in type 2 diabetes."
      Awata T., Inoue K., Kurihara S., Ohkubo T., Watanabe M., Inukai K., Inoue I., Katayama S.
      Diabetes 51:1635-1639(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN MICROVASCULAR COMPLICATIONS OF DIABETES.
    30. "VEGF165b, an inhibitory vascular endothelial growth factor splice variant: mechanism of action, in vivo effect on angiogenesis and endogenous protein expression."
      Woolard J., Wang W.-Y., Bevan H.S., Qiu Y., Morbidelli L., Pritchard-Jones R.O., Cui T.-G., Sugiono M., Waine E., Perrin R., Foster R., Digby-Bell J., Shields J.D., Whittles C.E., Mushens R.E., Gillatt D.A., Ziche M., Harper S.J., Bates D.O.
      Cancer Res. 64:7822-7835(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION (ISOFORM VEGF165B).
    31. "Control of the vascular endothelial growth factor internal ribosome entry site (IRES) activity and translation initiation by alternatively spliced coding sequences."
      Bornes S., Boulard M., Hieblot C., Zanibellato C., Iacovoni J.S., Prats H., Touriol C.
      J. Biol. Chem. 279:18717-18726(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING (ISOFORMS L-VEGF121; L-VEGF165 AND L-VEGF189).
    32. "Nuclear localization of long-VEGF is associated with hypoxia and tumor angiogenesis."
      Rosenbaum-Dekel Y., Fuchs A., Yakirevich E., Azriel A., Mazareb S., Resnick M.B., Levi B.Z.
      Biochem. Biophys. Res. Commun. 332:271-278(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING (ISOFORMS L-VEGF121 AND L-VEGF165), PROCESSING, SUBCELLULAR LOCATION.
    33. "Minimal active domain and mechanism of action of the angiogenesis inhibitor histidine-rich glycoprotein."
      Dixelius J., Olsson A.K., Thulin A., Lee C., Johansson I., Claesson-Welsh L.
      Cancer Res. 66:2089-2097(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CELL MIGRATION.
    34. "RSUME is implicated in HIF-1-induced VEGF-A production in pituitary tumour cells."
      Shan B., Gerez J., Haedo M., Fuertes M., Theodoropoulou M., Buchfelder M., Losa M., Stalla G.K., Arzt E., Renner U.
      Endocr. Relat. Cancer 19:13-27(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, INDUCTION.
    35. "Vascular endothelial growth factor: crystal structure and functional mapping of the kinase domain receptor binding site."
      Muller Y.A., Li B., Christinger H.W., Wells J.A., Cunningham B.C., de Vos A.M.
      Proc. Natl. Acad. Sci. U.S.A. 94:7192-7197(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 34-135.
    36. "1H, 13C, and 15N backbone assignment and secondary structure of the receptor-binding domain of vascular endothelial growth factor."
      Fairbrother W.J., Champe M.A., Christinger H.W., Keyt B.A., Starovasnik M.A.
      Protein Sci. 6:2250-2260(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 34-135.
    37. "The crystal structure of vascular endothelial growth factor (VEGF) refined to 1.93-A resolution: multiple copy flexibility and receptor binding."
      Muller Y.A., Christinger H.W., Keyt B.A., de Vos A.M.
      Structure 5:1325-1338(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 34-135.
    38. Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 39-134.
    39. "Solution structure of the heparin-binding domain of vascular endothelial growth factor."
      Fairbrother W.J., Champe M.A., Christinger H.W., Keyt B.A., Starovasnik M.A.
      Structure 6:637-648(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 137-215.

    Entry informationi

    Entry nameiVEGFA_HUMAN
    AccessioniPrimary (citable) accession number: P15692
    Secondary accession number(s): B5BU86
    , H0Y2S8, H0Y407, H0Y414, H0Y462, H0Y8N2, H3BLW7, O60720, O75875, Q074Z4, Q16889, Q5UB46, Q6P0P5, Q96KJ0, Q96L82, Q96NW5, Q9H1W8, Q9H1W9, Q9UH58, Q9UL23
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: November 16, 2001
    Last modified: October 1, 2014
    This is version 195 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3